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Self-Assembly of Hydrogels From Elastin-Mimetic Block Copolymers

  • Elizabeth R. Wright (a1), R. Andrew McMillan (a1), Alan Cooper (a2), Robert P. Apkarian (a3) and Vincent P. Conticello (a1)...


Triblock copolymers have traditionally been synthesized with conventional organic components. However, triblock copolymers could be synthesized by the incorporation of two incompatible protein-based polymers. The polypeptides would differ in their hydrophobicity and confer unique physiochemical properties to the resultant materials. One protein-based polymer, based on a sequence of native elastin, that has been utilized in the synthesis of biomaterials is poly (Valine-Proline-Glycine-ValineGlycine) or poly(VPGVG) [1]. This polypeptide has been shown to have an inverse temperature transition that can be adjusted by non-conservative amino acid substitutions in the fourth position [2]. By combining polypeptide blocks with different inverse temperature transition values due to hydrophobicity differences, we expect to produce amphiphilic polypeptides capable of self-assembly into hydrogels. Our research examines the design, synthesis and characterization of elastin-mimetic block copolymers as functional biomaterials. The methods that are used for the characterization include variable temperature 1D and 2D High-Resolution-NMR, cryo-High Resolutions Scanning Electron Microscopy and Differential Scanning Calorimetry.



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1. Urry, D.W., Luan, C.H., Harrris, C.M., Parker, T.M., (1997) Protein-based materials with a profound range of properties and applications: The elastin ΔTt hydrophobic paradigm, Protein-Based Materials, 133-177.
2. Urry, D.W., (1988) Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics, J. Protein Chem., 7, 134.
3. Urry, D.W., (1991) Protein folding controlled by chemically shifting the temperatures of inverse temperature transitions, Proteins: Structure, dynamics and design, 352360.
4. Kleppinger, R., Mischenko, N., Theunissen, E., Reynaers, H.L., Koch, M.H.J., Almdal, K., and Mortensen, K. (1997) Shear-induced single crystalline mesophases in physical networks of gel-forming triblock copolymer solutions, Macromolecules, 30, 70127014.
5. Sambook, J., Fritsch, E. F., Maniatis, T., Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory Press: Cold Spring Harbor: NY, 1989.
6. Lee, T.A.T, Cooper, A., Apkarian, R. P., Conticello, V.P., (2000) Thermo-reversible self-assembly of nanoparticles derived from elastin-mimetic polypeptides, Advanced Materials, 12, 11051110.
7. Wright, E. R., McMillan, R. A., Cooper, A., Apkarian, R. P., and Conticello, V. P.. Thermoplastic Elastomer Hydrogels via Self-Assembly of an Elastin-Mimetic Triblock Polypeptide. Advanced Functional Materials, 12 (2), 149154 (2002).
8. McMillan, R.A., Lee, T.A.T., Conticello, V.P., (1999) Rapid assembly of synthetic genes encoding protein polymers, Macromolecules, 32, 36433648.
9. Daniell, H., Guda, C., McPherson, D., Zhang, X., Urry, D.W., (1996) Hyperexpression of a synthetic protein-based polymer gene, Methods in Molecular Biology, 63, 359371.
10. McMillan, R.A., Conticello, V.P., (2000) Synthesis and characterization of elastinmimetic protein gels derived from a well-defined polypeptide precursor. Macromolecules, 30, 48094821.
11. Wishart, D.S., Sykes, B.D (1994) The 13C-chemical shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data, J. Bio NMR, 171180.
12. Wishart, D.S., Bigam, C.G., Holm, A., Hodges, R.S., Sykes, B.D., (1995) 1H, 13C, 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of near-neighbor effects, J. Bio NMR, 6781.
13. McMillan, R.A., Caran, K., Apkarian, R.P., Conticello, V.P., (1999), High-Resolution topographic imaging of environmentally responsive, elastin-mimetic hydrogels, Macromolecules, 32, 90679070.
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